ID   NIA_ASPNG               Reviewed;         867 AA.
AC   P36858;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   25-NOV-2008, entry version 64.
DE   RecName: Full=Nitrate reductase [NADPH];
DE            Short=NR;
DE            EC=1.7.1.3;
GN   Name=niaD;
OS   Aspergillus niger.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae;
OC   mitosporic Trichocomaceae; Aspergillus.
OX   NCBI_TaxID=5061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=92175518; PubMed=1541396; DOI=10.1016/0378-1119(92)90682-F;
RA   Unkles S.E., Campbell E.I., Punt P.J., Hawker K.L., Contreras R.,
RA   Hawkins A.R., van den Hondel C.A.M.J.J., Kinghorn J.R.;
RT   "The Aspergillus niger niaD gene encoding nitrate reductase: upstream
RT   nucleotide and amino acid sequence comparisons.";
RL   Gene 111:149-155(1992).
CC   -!- FUNCTION: Nitrate reductase is a key enzyme involved in the first
CC       step of nitrate assimilation in plants, fungi and bacteria.
CC   -!- CATALYTIC ACTIVITY: Nitrite + NADP(+) + H(2)O = nitrate + NADPH.
CC   -!- COFACTOR: Binds 1 FAD.
CC   -!- COFACTOR: Binds 1 heme group. The heme group is called cytochrome
CC       b-557.
CC   -!- COFACTOR: Binds 1 molybdenum ion.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SIMILARITY: Belongs to the nitrate reductase family.
CC   -!- SIMILARITY: Contains 1 cytochrome b5 heme-binding domain.
CC   -!- SIMILARITY: Contains 1 FAD-binding FR-type domain.
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DR   EMBL; M77022; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; JQ1525; JQ1525.
DR   HSSP; P17571; 2CND.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0050660; F:FAD binding; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR   GO; GO:0050464; F:nitrate reductase (NADPH) activity; IEA:EC.
DR   GO; GO:0042128; P:nitrate assimilation; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR001199; Cyt_B5.
DR   InterPro; IPR001834; Cyt_B5_reductase.
DR   InterPro; IPR001709; FPN_cyt_redctse.
DR   InterPro; IPR005066; MoCF_OxRdtse_dimer.
DR   InterPro; IPR008335; Mopterin_OxRdtase_euk.
DR   InterPro; IPR012137; Nitr_rd_NADH.
DR   InterPro; IPR008333; OxRdtase_FAD-bd.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD_bd.
DR   InterPro; IPR000572; OxRdtase_Mopterin-bd.
DR   Gene3D; G3DSA:3.10.120.10; Cyt_B5; 1.
DR   Gene3D; G3DSA:2.60.40.650; MoCF_oxrdtse_dimer; 1.
DR   Gene3D; G3DSA:3.90.420.10; Oxred_molyb_bd; 1.
DR   Pfam; PF00173; Cyt-b5; 1.
DR   Pfam; PF00970; FAD_binding_6; 1.
DR   Pfam; PF03404; Mo-co_dimer; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   Pfam; PF00174; Oxidored_molyb; 1.
DR   PIRSF; PIRSF000233; Nitr_rd_NADH; 1.
DR   PRINTS; PR00406; CYTB5RDTASE.
DR   PRINTS; PR00363; CYTOCHROMEB5.
DR   PRINTS; PR00407; EUMOPTERIN.
DR   PRINTS; PR00371; FPNCR.
DR   ProDom; PD000612; Cyt_B5; 1.
DR   PROSITE; PS00191; CYTOCHROME_B5_1; 1.
DR   PROSITE; PS50255; CYTOCHROME_B5_2; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
DR   PROSITE; PS00559; MOLYBDOPTERIN_EUK; 1.
PE   3: Inferred from homology;
KW   FAD; Flavoprotein; Heme; Iron; Metal-binding; Molybdenum; NADP;
KW   Nitrate assimilation; Oxidoreductase.
FT   CHAIN         1    867       Nitrate reductase [NADPH].
FT                                /FTId=PRO_0000166040.
FT   DOMAIN      514    589       Cytochrome b5 heme-binding.
FT   DOMAIN      615    726       FAD-binding FR-type.
FT   NP_BIND     837    846       NADP (By similarity).
FT   METAL       152    152       Molybdenum-pterin (Potential).
FT   METAL       203    203       Molybdenum-pterin (Potential).
FT   METAL       549    549       Iron (heme axial ligand) (By similarity).
FT   METAL       572    572       Iron (heme axial ligand) (By similarity).
FT   DISULFID    399    399       Interchain (Potential).
SQ   SEQUENCE   867 AA;  97189 MW;  BE40335DCBE12E42 CRC64;
     MATVTEVLTE PFTAQGVTLK SGPIKVHQEE LPAVELSDIP LPPPSKEPTE VLSIDKPTPD
     YHVPRDPRLI RLTGVHPFNV EPPLTALYDE GFLTSPELFY VRNHGPVPLV KDEDIPNWEI
     SIEGLVEKPL VLNFRDILQQ YDQITAPITL VCAGNRRKEQ NVVRKTKGFS WGSAGLSTAL
     WTGPMMADIL RSAKPLRKAK YVCMEGADKL PNGYYGTSIK LNWAMDPNRG IMLAHKMNGE
     DLRPDHGRPL RAVVPGQIGG RSVKWLKKLI LTDAPSDNWY HIYDNRVLPT MVSPEMSSSD
     PNWWRDDRYA IYDLNVNSSV VYPEHKEVLD LASAGPSYNV KGYAYAGGGR RITRVEISLD
     KGKSWRLANI SYAEDKYRDF EGDLFGGRVH MSWRETCFCW CFWSLDIAIP ELENTDAILV
     RAMDEALALQ PRDMYWSVLG MMNNPWFRVT ITKENGTLRF EHPTDPTGPG GWMERVKKAG
     GDLVNGYWGE RQAGEEPTEP EPEKEINMKK EGVNRIIDLQ EFKKNSSDEK PWFIVNGEVY
     DGTAFLEGHP GGAQSIISSA GIDVSEEFLA IHTQTAKAMM PDYHIGTMDK ASLEALKNDN
     APQSDEPRAT FLQSKSWTKA TLVKRTDVSW DTRIFTFQLQ HDKQTLGLPI GQHLMIKVAD
     PTSKEAIIRS YTPISDTNQE GTMDLLVKIY FDTPTVKGGK MTMALEKLAL GSEIDCKGPT
     GRFEYLGNGK ILVSGKERHV SSFKMICGGT GITPIFQVLR AVMQDKQDPT SCVVLDGNRQ
     EEDILCRADL DAYEALDSKK CKVVHTLTKA PDSWTGRRGR ISEDLLKEHA IPDGKSMVLI
     CGPEAMEKSA RKILLEQGWA ESDLHFF
//